Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.

  title={Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.},
  author={N. Esaki and T. Nakamura and H. Tanaka and K. Soda},
  journal={The Journal of biological chemistry},
  volume={257 8},
We have found a novel enzyme that exclusively decomposes L-selenocysteine into L-alanine and H2Se in various mammalian tissues, and have named it selenocysteine lyase. The enzyme from pig liver has been purified to homogeneity. It has a molecular weight of approximately 85,000, and contains pyridoxal 5'-phosphate as a coenzyme. Its maximum reactivity is at about pH 9.0. Balance studies showed that 1 mol of selenocysteine is converted to equimolar amounts of alanine and H2Se. The following amino… Expand
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The purification and characterization of bacterial selenocysteine beta-lyase, an enzyme which specifically catalyzes the cleavage of L-selenocysteines to L-alanine and Se0, are presented and the catalytic properties are very similar. Expand
Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme
  • L. Seale
  • Chemistry, Medicine
  • Antioxidants
  • 2019
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Mechanism, Structure, and Biological Role of Selenocysteine Lyase
Selenocysteine lyase is a pyridoxal 5′-phosphate-dependent enzyme catalyzing the degradation of l-selenocysteine to l-alanine and elemental selenium. It is unique in that it acts exclusively onExpand
Mechanism of reactions catalyzed by selenocysteine β-Lyase
Abstract The reaction mechanism of selenocystine β-lyase has been studied and it was found that elemental selenium is released enzymatically from selenocysteine, and reduced to H2Se nonenzymaticallyExpand